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Database: UniProt
Entry: A0A1S2ZCY8_ERIEU
LinkDB: A0A1S2ZCY8_ERIEU
Original site: A0A1S2ZCY8_ERIEU 
ID   A0A1S2ZCY8_ERIEU        Unreviewed;       961 AA.
AC   A0A1S2ZCY8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Dynamin-like 120 kDa protein, mitochondrial {ECO:0000256|ARBA:ARBA00018307};
DE            EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN   Name=OPA1 {ECO:0000313|RefSeq:XP_007517474.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007517474.1};
RN   [1] {ECO:0000313|RefSeq:XP_007517474.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001837};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004434}. Mitochondrion membrane
CC       {ECO:0000256|ARBA:ARBA00004325}.
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DR   RefSeq; XP_007517474.1; XM_007517412.1.
DR   AlphaFoldDB; A0A1S2ZCY8; -.
DR   CTD; 4976; -.
DR   OrthoDB; 48011at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   CDD; cd08771; DLP_1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR022812; Dynamin.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR045817; OPA1_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11566; DYNAMIN; 1.
DR   PANTHER; PTHR11566:SF67; DYNAMIN-LIKE 120 KDA PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF19434; OPA1_C; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
PE   4: Predicted;
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          286..562
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   COILED          171..254
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          897..924
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   961 AA;  111649 MW;  DCC1D9CED469C648 CRC64;
     MWRLRRAAVA CEVCQSLVKH SSGVKGSIPL QKLHLVSRSI YHSHHPTIKL QRPQLRMSLQ
     QFSSLTNLPL RKSKISPMKY GYQPRRNFWP ARLAARLLKL RYLILGSAVG GGYTAKKTFD
     QWKDMIPDLS DYKWIVPDIV WEIDEYIDLG SSGETAFRAT EHGSENDKHY RKGLLGELIL
     LQQQIQEHEE EARRAAGQYN TSYAQQKRKV SDKEKIDQLQ EELLHTQLKY QRILERLEKE
     NKELRKIVLQ KDDKGIHHRK LKKSLIDMYS EVLDVLSDYD ASYNTQDHLP RVVVVGDQSA
     GKTSVLEMIA QARIFPRGSG EMMTRSPVKV TLSEGPHHVA LFKDSSREFD LTKEEDLAAL
     RHEIELRMRK NVKEGCTVSP ETISLNVKGP GLQRMVLVDL PGVINTVTAG MAPDTKETIF
     SISKAYMQNP NAIILCIQDG SVDAERSIVT DLVSQMDPHG RRTIFVLTKV DLAEKNVASP
     SRIQQIIEGK LFPMKALGYF AVVTGKGNSS ESIEAIREYE EEFFQNSKLL KTSMLKAHQV
     TTRNLSLAVS DCFWKMVRES VEQQADSFKA TRFNLETEWK NNYPRLRELD RNELFEKAKN
     EILDEVISLS QVTPKHWEEI LQQSLWERVS THVIENIYLP AAQTMNSGTF NTTVDIKLKQ
     WTDKQLPNKA VEVAWETLQE EFSRFMTEPK GKEHDDIFDK LKEAVKEESI KRHKWNDFAE
     DSLRVIQHNA LEDRSISDKQ QWDAAIYFME EALQARLKDT EDAIENMIGP DWKKRWLYWK
     NRTQEQGIHN ETKNELEKML KCNEEHPAYL ASDEITTVRK NLESRGVEVD PSLIKDTWHQ
     VYRRHFLKTA LNHCNLCRRG FYYYQRHFVD SELECNDVVL FWRIQRMLAI TANTLRQQLT
     NTEVRRLEKN VKEVLEDFAE DSEKKVKLLT GKRVQLAEDL KKVREIQEKL DAFIEALHQE
     K
//
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